Donghan Lee

1.9k total citations
49 papers, 1.4k citations indexed

About

Donghan Lee is a scholar working on Molecular Biology, Spectroscopy and Biophysics. According to data from OpenAlex, Donghan Lee has authored 49 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Molecular Biology, 20 papers in Spectroscopy and 9 papers in Biophysics. Recurrent topics in Donghan Lee's work include Protein Structure and Dynamics (21 papers), Advanced NMR Techniques and Applications (11 papers) and Electron Spin Resonance Studies (9 papers). Donghan Lee is often cited by papers focused on Protein Structure and Dynamics (21 papers), Advanced NMR Techniques and Applications (11 papers) and Electron Spin Resonance Studies (9 papers). Donghan Lee collaborates with scholars based in Germany, United States and Switzerland. Donghan Lee's co-authors include Christian Griesinger, Stefan Becker, Christian Hilty, Kurt Wüthrich, Gerhard Wider, T. Michael Sabo, David Ban, Korvin F. A. Walter, Konstantin Pervushin and R. Bryn Fenwick and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Donghan Lee

49 papers receiving 1.4k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Donghan Lee Germany 21 936 415 232 158 148 49 1.4k
Ewen Lescop France 24 1.3k 1.3× 322 0.8× 248 1.1× 136 0.9× 115 0.8× 59 1.9k
Fang Tian United States 23 1.1k 1.1× 446 1.1× 322 1.4× 72 0.5× 149 1.0× 59 1.5k
Zach Serber United States 16 1.3k 1.4× 388 0.9× 293 1.3× 81 0.5× 143 1.0× 17 1.7k
Arthur M. Mandel United States 10 982 1.0× 316 0.8× 307 1.3× 73 0.5× 121 0.8× 15 1.3k
Vladimir J. Basus United States 23 908 1.0× 303 0.7× 167 0.7× 102 0.6× 91 0.6× 40 1.3k
Leszek Poppe United States 26 1.4k 1.5× 330 0.8× 228 1.0× 101 0.6× 111 0.8× 55 2.1k
Wladimir Labeikovsky United States 10 1.1k 1.1× 247 0.6× 315 1.4× 65 0.4× 137 0.9× 10 1.3k
Masaki Mishima Japan 24 1.2k 1.3× 244 0.6× 239 1.0× 116 0.7× 119 0.8× 55 1.5k
Gregg Siegal Netherlands 27 1.7k 1.9× 284 0.7× 305 1.3× 136 0.9× 120 0.8× 59 2.2k
Hitoshi Kuboniwa United States 13 1.4k 1.5× 310 0.7× 424 1.8× 81 0.5× 146 1.0× 24 1.8k

Countries citing papers authored by Donghan Lee

Since Specialization
Citations

This map shows the geographic impact of Donghan Lee's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Donghan Lee with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Donghan Lee more than expected).

Fields of papers citing papers by Donghan Lee

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Donghan Lee. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Donghan Lee. The network helps show where Donghan Lee may publish in the future.

Co-authorship network of co-authors of Donghan Lee

This figure shows the co-authorship network connecting the top 25 collaborators of Donghan Lee. A scholar is included among the top collaborators of Donghan Lee based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Donghan Lee. Donghan Lee is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Tak, Sungho, Eunha Hwang, Donghan Lee, et al.. (2023). Kinetic evidence in favor of glyoxalase III and against deglycase activity of DJ‐1. Protein Science. 32(5). e4641–e4641. 8 indexed citations
2.
Kim, Boram, Vytautas Gapsys, Jun‐Goo Jee, et al.. (2021). Repositioning Food and Drug Administration-Approved Drugs for Inhibiting Biliverdin IXβ Reductase B as a Novel Thrombocytopenia Therapeutic Target. Journal of Medicinal Chemistry. 65(3). 2548–2557. 3 indexed citations
3.
Jin, Zeyu, et al.. (2020). Characteristic Analysis of Homo- and Heterodimeric Complexes of Human Mitochondrial Pyruvate Carrier Related to Metabolic Diseases. International Journal of Molecular Sciences. 21(9). 3403–3403. 12 indexed citations
4.
Smith, Colin A., Artur Mazur, Ashok K. Rout, et al.. (2019). Enhancing NMR derived ensembles with kinetics on multiple timescales. Journal of Biomolecular NMR. 74(1). 27–43. 10 indexed citations
5.
Sabo, T. Michael, Vytautas Gapsys, Korvin F. A. Walter, et al.. (2018). Utilizing dipole-dipole cross-correlated relaxation for the measurement of angles between pairs of opposing CαHα-CαHα bonds in anti-parallel β-sheets. Methods. 138-139. 85–92. 3 indexed citations
6.
Pratihar, Supriya, T. Michael Sabo, David Ban, et al.. (2016). Kinetics of the Antibody Recognition Site in the Third IgG‐Binding Domain of Protein G. Angewandte Chemie International Edition. 55(33). 9567–9570. 22 indexed citations
7.
Pratihar, Supriya, T. Michael Sabo, David Ban, et al.. (2016). Kinetics of the Antibody Recognition Site in the Third IgG‐Binding Domain of Protein G. Angewandte Chemie. 128(33). 9719–9722. 5 indexed citations
8.
Ban, David, et al.. (2016). High-power 1 H composite pulse decoupling provides artifact free exchange-mediated saturation transfer (EST) experiments. Journal of Magnetic Resonance. 269. 65–69. 7 indexed citations
9.
Pilger, Jens, Artur Mazur, Peter Monecke, et al.. (2015). A Combination of Spin Diffusion Methods for the Determination of Protein–Ligand Complex Structural Ensembles. Angewandte Chemie International Edition. 54(22). 6511–6515. 16 indexed citations
10.
Koharudin, Leonardus M. I., David Ban, T. Michael Sabo, et al.. (2015). Sampling of Glycan‐Bound Conformers by the Anti‐HIV Lectin Oscillatoria agardhii agglutinin in the Absence of Sugar. Angewandte Chemie International Edition. 54(22). 6462–6465. 12 indexed citations
11.
Griesinger, Christian, et al.. (2015). Speeding-up exchange-mediated saturation transfer experiments by Fourier transform. Journal of Biomolecular NMR. 63(3). 237–244. 10 indexed citations
12.
Kim, Do Hyoung, Chewook Lee, Si‐Hyung Lee, et al.. (2014). A pre-structured helix in the intrinsically disordered 4EBP1. Molecular BioSystems. 11(2). 366–369. 10 indexed citations
13.
Edwards, Luke, et al.. (2014). Quantum mechanical NMR simulation algorithm for protein-size spin systems. Journal of Magnetic Resonance. 243. 107–113. 30 indexed citations
14.
Michielssens, Servaas, David Ban, Supriya Pratihar, et al.. (2014). A Designed Conformational Shift To Control Protein Binding Specificity. Angewandte Chemie International Edition. 53(39). 10367–10371. 46 indexed citations
15.
Mazur, Artur, et al.. (2013). ShereKhan—calculating exchange parameters in relaxation dispersion data from CPMG experiments. Bioinformatics. 29(14). 1819–1820. 16 indexed citations
16.
Ban, David, Artur Mazur, T. Michael Sabo, et al.. (2013). Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy. Journal of Biomolecular NMR. 57(1). 73–82. 21 indexed citations
17.
Ko, Hyun‐Chang, et al.. (2012). Comparative analysis of the use of complementary and alternative medicine by Korean patients with androgenetic alopecia, atopic dermatitis and psoriasis. Journal of the European Academy of Dermatology and Venereology. 27(7). 827–835. 26 indexed citations
18.
Ban, David, Alvar D. Gossert, Karin Giller, et al.. (2012). Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead. Journal of Magnetic Resonance. 221. 1–4. 54 indexed citations
19.
Michel, Erich, Fred F. Damberger, Yuko Ishida, et al.. (2011). Dynamic Conformational Equilibria in the Physiological Function of the Bombyx mori Pheromone-Binding Protein. Journal of Molecular Biology. 408(5). 922–931. 25 indexed citations
20.
Lee, Donghan, Joseph D. Walsh, Ping Yu, et al.. (2007). The Structure of Free L11 and Functional Dynamics of L11 in Free, L11-rRNA(58 nt) Binary and L11-rRNA(58 nt)-thiostrepton Ternary Complexes. Journal of Molecular Biology. 367(4). 1007–1022. 29 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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